Two-Component Signal Transduction in
            <i>Bacillus subtilis</i>
            : How One Organism Sees Its World

Fabret, Céline; Feher, Victoria A.; Hoch, James A.

doi:10.1128/jb.181.7.1975-1983.1999

Cited by 336 publications

(177 citation statements)

References 33 publications

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“…A comparison of signal transduction proteins is given in Table 2. Rap family aspartate phosphatases [17]. SK, sensor histidine kinase; RR, response regulator; ECF, extra cytoplasmic function.…”

Section: Comparative Signal Transduction System Analysismentioning

confidence: 99%

Comparative genome analysis ofBacillus cereusgroup genomes withBacillus subtilis

Anderson

Sorokin

Kapatral

et al. 2005

FEMS Microbiology Letters

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Genome features of the Bacillus cereus group genomes (representative strains of Bacillus cereus, Bacillus anthracis and Bacillus thuringiensis sub spp. israelensis) were analyzed and compared with the Bacillus subtilis genome. A core set of 1381 protein families among the four Bacillus genomes, with an additional set of 933 families common to the B. cereus group, was identified. Differences in signal transduction pathways, membrane transporters, cell surface structures, cell wall, and S-layer proteins suggesting differences in their phenotype were identified. The B. cereus group has signal transduction systems including a tyrosine kinase related to two-component system histidine kinases from B. subtilis. A model for regulation of the stress responsive sigma factor sigmaB in the B. cereus group different from the well studied regulation in B. subtilis has been proposed. Despite a high degree of chromosomal synteny among these genomes, significant differences in cell wall and spore coat proteins that contribute to the survival and adaptation in specific hosts has been identified.

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Section: Comparative Signal Transduction System Analysismentioning

confidence: 99%

Comparative genome analysis ofBacillus cereusgroup genomes withBacillus subtilis

Anderson

Sorokin

Kapatral

et al. 2005

FEMS Microbiology Letters

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“…HAMP linkers are variable in length (40-180 residues) and have a predicted topology of two amphipathic helices separated by a loop region. They have been hypothesized to transmit signals between the external input domain and the cytoplasmic output module (Fabret et al, 1999;Williams and Stewart, 1999).…”

Section: Introductionmentioning

confidence: 99%

Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein

Marina

Waldburger

Hendrickson

2005

EMBO J

273

341

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The large majority of histidine kinases (HKs) are multifunctional enzymes having autokinase, phosphotransfer and phosphatase activities, and most of these are transmembrane sensor proteins. Sensor HKs possess conserved cytoplasmic phosphorylation and ATP-binding kinase domains. The different enzymatic activities require participation by one or both of these domains, implying the need for different conformational states. The catalytic domains are linked to the membrane through a coiledcoil segment that sometimes includes other domains. We describe here the first crystal structure of the complete cytoplasmic region of a sensor HK, one from the thermophile Thermotoga maritima in complex with ADPbN at 1.9 Å resolution. The structure reveals previously unidentified functions for several conserved residues and reveals the relative disposition of domains in a state seemingly poised for phosphotransfer. The structure thereby inspires hypotheses for the mechanisms of autophosphorylation, phosphotransfer and response-regulator dephosphorylation, and for signal transduction through the coiled-coil segment. Mutational tests support the functional relevance of interdomain contacts.

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“…About 20 years ago, Fabret, Feher and Hoch published a minireview on two-component signal transduction in Bacillus subtilis with a provocative subtitle 'How one organism sees its world'. Making use of the just-finished complete genome sequence of B. subtilis strain 168, they examined 36 histidine kinases (HKs) and 35 response regulators (RRs) encoded in this genome and classified them into several groups based on the organization of the conserved motifs surrounding phosphoacceptor His residues in HKs and Asp residues in RRs (Fabret et al, 1999). The same year, a joint paper from Saier and Stülke labs provided a careful analysis of the components of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) encoded in B. subtilis (Reizer et al, 1999), while we presented an account of the 3 0 ,5 0 -cyclic dimeric guanosine monophosphate (c-di-GMP)-related GGDEF, EAL and HD-GYP domains in several model genomes .…”

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confidence: 99%

What bacteria want

Galperin

2018

Environmental Microbiology

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Bacterial signal transduction systems are responsible for sensing environmental cues and adjusting the cellular behaviour and/or metabolism in response to these cues. They also monitor the intracellular conditions and the status of the cell envelope and the cytoplasmic membrane and trigger various stress responses to counteract adverse changes. This surveillance involves several classes of sensor proteins: histidine kinases; chemoreceptors; membrane components of the sugar phosphotransferase system; adenylate, diadenylate and diguanylate cyclases and certain cAMP, c-di-AMP and c-di-GMP phosphodiesterases; extracytoplasmic function sigma factors and Ser/Thr/Tyr protein kinases and phosphoprotein phosphatases. We have compiled a detailed listing of sensor proteins that are encoded in the genomes of Escherichia coli, Bacillus subtilis and 10 widespread pathogens: Chlamydia trachomatis, Haemophilus influenzae, Helicobacter pylori, Mycobacterium tuberculosis, Mycoplasma pneumoniae, Neisseria gonorrhoeae, Porphyromonas gingivalis, Rickettsia typhi, Streptococcus pyogenes and Treponema pallidum, and checked what, if anything, is known about their functions. This listing shows significant gaps in the understanding of which environmental and intracellular cues are perceived by these bacteria and which cellular responses are triggered by the changes in the respective parameters. A better understanding of bacterial preferences may suggest new ways to modulate the expression of virulence factors and therefore decrease the reliance on antibiotics to fight infection.

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Two-Component Signal Transduction in Bacillus subtilis : How One Organism Sees Its World

Cited by 336 publications

References 33 publications

Comparative genome analysis ofBacillus cereusgroup genomes withBacillus subtilis

Comparative genome analysis ofBacillus cereusgroup genomes withBacillus subtilis

Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein

What bacteria want

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